Sequence-ensemble relationships of intrinsically disordered proteins (IDPs) are governed by binary patterns such as the linear clustering or mixing of specific residues or residue …
Intrinsically disordered regions (IDRs) defying the traditional protein structure–function paradigm have been difficult to analyze. The availability of accurate structure predictions on …
S Chong, M Mir - Journal of molecular biology, 2021 - Elsevier
A substantial portion of the proteome consists of intrinsically disordered regions (IDRs) that do not fold into well-defined 3D structures yet perform numerous biological functions and are …
The development of AlphaFold2 marked a paradigm-shift in the structural biology community. Herein, we assess the ability of AlphaFold2 to predict disordered regions …
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are fascinating dynamic conformational ensembles that are observed under physiological …
Protein structures can provide invaluable information, both for reasoning about biological processes and for enabling interventions such as structure-based drug development or …
CJ Oldfield, AK Dunker - Annual review of biochemistry, 2014 - annualreviews.org
Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities. Their mobile flexibility and structural instability are encoded …
The AlphaFold Protein Structure Database contains predicted structures for millions of proteins. For the majority of human proteins that contain intrinsically disordered regions …
Intrinsically disordered regions in proteins are relatively frequent and important for our understanding of molecular recognition and assembly, and protein structure and function …